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Cathepsin L1 (EC 3.4.22.15) (Cathepsin L) (Major excreted protein) (MEP) [Cleaved into: Cathepsin L1 heavy chain; Cathepsin L1 light chain]

 CATL1_HUMAN             Reviewed;         333 AA.
P07711; Q6IAV1; Q96QJ0;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
25-OCT-2017, entry version 198.
RecName: Full=Cathepsin L1;
EC=3.4.22.15;
AltName: Full=Cathepsin L;
AltName: Full=Major excreted protein;
Short=MEP;
Contains:
RecName: Full=Cathepsin L1 heavy chain;
Contains:
RecName: Full=Cathepsin L1 light chain;
Flags: Precursor;
Name=CTSL; Synonyms=CTSL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3421948; DOI=10.1042/bj2530303;
Gal S., Gottesman M.M.;
"Isolation and sequence of a cDNA for human pro-(cathepsin L).";
Biochem. J. 253:303-306(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2835398; DOI=10.1172/JCI113497;
Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.;
"Complete nucleotide and deduced amino acid sequences of human and
murine preprocathepsin L. An abundant transcript induced by
transformation of fibroblasts.";
J. Clin. Invest. 81:1621-1629(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 114-288 AND 292-333.
PubMed=3342889; DOI=10.1016/0014-5793(88)80028-0;
Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.;
"Amino acid sequences of the human kidney cathepsins H and L.";
FEBS Lett. 228:341-345(1988).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 113-154.
PubMed=3550705; DOI=10.1093/nar/15.7.3186;
Joseph L.J., Lapid S., Sukhatme V.P.;
"The major ras induced protein in NIH3T3 cells is cathepsin L.";
Nucleic Acids Res. 15:3186-3186(1987).
[9]
PROTEIN SEQUENCE OF 114-154 AND 292-333.
PubMed=3545185; DOI=10.1042/bj2400373;
Mason R.W., Walker J.E., Northrop F.D.;
"The N-terminal amino acid sequences of the heavy and light chains of
human cathepsin L. Relationship to a cDNA clone for a major cysteine
proteinase from a mouse macrophage cell line.";
Biochem. J. 240:373-377(1986).
[10]
GLYCOSYLATION AT ASN-221.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-333.
PubMed=8896443;
Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S.,
Cygler M.;
"Structure of human procathepsin L reveals the molecular basis of
inhibition by the prosegment.";
EMBO J. 15:5492-5503(1996).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-333.
PubMed=9141479; DOI=10.1016/S0014-5793(97)00216-0;
Fujishima A., Imai Y., Nomura T., Fujisawa Y., Yamamoto Y.,
Sugarawa T.;
"The crystal structure of human cathepsin L complexed with E-64.";
FEBS Lett. 407:47-50(1997).
[18]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-333.
Cygler M., Coulombe R.;
Submitted (AUG-1999) to the PDB data bank.
-!- FUNCTION: Important for the overall degradation of proteins in
lysosomes.
-!- CATALYTIC ACTIVITY: Specificity close to that of papain. As
compared to cathepsin B, cathepsin L exhibits higher activity
toward protein substrates, but has little activity on Z-Arg-Arg-
NHMec, and no peptidyl-dipeptidase activity.
-!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide
bonds.
-!- INTERACTION:
O43765:SGTA; NbExp=3; IntAct=EBI-1220160, EBI-347996;
G5EFH4:srp-6 (xeno); NbExp=2; IntAct=EBI-1220160, EBI-1549936;
-!- SUBCELLULAR LOCATION: Lysosome.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CTSL1ID40208ch9q21.html";
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EMBL; X12451; CAA30981.1; -; mRNA.
EMBL; M20496; AAA66974.1; -; mRNA.
EMBL; CR457053; CAG33334.1; -; mRNA.
EMBL; BX537395; CAD97637.1; -; mRNA.
EMBL; AL160279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012612; AAH12612.1; -; mRNA.
EMBL; X05256; CAA28877.1; -; mRNA.
CCDS; CCDS6675.1; -.
PIR; S01002; KHHUL.
RefSeq; NP_001244900.1; NM_001257971.1.
RefSeq; NP_001244901.1; NM_001257972.1.
RefSeq; NP_001903.1; NM_001912.4.
RefSeq; NP_666023.1; NM_145918.2.
RefSeq; XP_005251773.1; XM_005251716.3.
UniGene; Hs.731507; -.
PDB; 1CJL; X-ray; 2.20 A; A=22-333.
PDB; 1CS8; X-ray; 1.80 A; A=19-333.
PDB; 1ICF; X-ray; 2.00 A; A/C=114-288, B/D=292-333.
PDB; 1MHW; X-ray; 1.90 A; A/B=114-288, C/D=292-333.
PDB; 2NQD; X-ray; 1.75 A; B=113-333.
PDB; 2VHS; X-ray; 1.50 A; A/B/C/D=114-285, A/B/C/D=294-333.
PDB; 2XU1; X-ray; 1.45 A; A/B/C/D=114-333.
PDB; 2XU3; X-ray; 0.90 A; A=114-333.
PDB; 2XU4; X-ray; 1.12 A; A=114-333.
PDB; 2XU5; X-ray; 1.60 A; A=114-333.
PDB; 2YJ2; X-ray; 1.15 A; A=114-333.
PDB; 2YJ8; X-ray; 1.30 A; A=114-333.
PDB; 2YJ9; X-ray; 1.35 A; A=114-333.
PDB; 2YJB; X-ray; 1.40 A; A=114-333.
PDB; 2YJC; X-ray; 1.14 A; A=114-333.
PDB; 3BC3; X-ray; 2.20 A; A/B=114-333.
PDB; 3H89; X-ray; 2.50 A; A/B/C/D/E/F=114-333.
PDB; 3H8B; X-ray; 1.80 A; A/B/C/D/E/F=114-333.
PDB; 3H8C; X-ray; 2.50 A; A/B=114-333.
PDB; 3HHA; X-ray; 1.27 A; A/B/C/D=114-333.
PDB; 3HWN; X-ray; 2.33 A; A/B/C/D=76-333.
PDB; 3IV2; X-ray; 2.20 A; A/B=114-333.
PDB; 3K24; X-ray; 2.50 A; A/B=114-333.
PDB; 3KSE; X-ray; 1.71 A; A/B/C=114-333.
PDB; 3OF8; X-ray; 2.20 A; A=113-333.
PDB; 3OF9; X-ray; 1.76 A; A=113-333.
PDB; 4AXL; X-ray; 1.92 A; A=114-333.
PDB; 4AXM; X-ray; 2.80 A; A/B/F/I/L/O=114-333.
PDB; 5F02; X-ray; 1.43 A; A=114-333.
PDB; 5I4H; X-ray; 1.42 A; A=113-218, B=222-333.
PDB; 5MAE; X-ray; 1.00 A; A=114-333.
PDB; 5MAJ; X-ray; 1.00 A; A=114-333.
PDB; 5MQY; X-ray; 1.13 A; A=114-333.
PDBsum; 1CJL; -.
PDBsum; 1CS8; -.
PDBsum; 1ICF; -.
PDBsum; 1MHW; -.
PDBsum; 2NQD; -.
PDBsum; 2VHS; -.
PDBsum; 2XU1; -.
PDBsum; 2XU3; -.
PDBsum; 2XU4; -.
PDBsum; 2XU5; -.
PDBsum; 2YJ2; -.
PDBsum; 2YJ8; -.
PDBsum; 2YJ9; -.
PDBsum; 2YJB; -.
PDBsum; 2YJC; -.
PDBsum; 3BC3; -.
PDBsum; 3H89; -.
PDBsum; 3H8B; -.
PDBsum; 3H8C; -.
PDBsum; 3HHA; -.
PDBsum; 3HWN; -.
PDBsum; 3IV2; -.
PDBsum; 3K24; -.
PDBsum; 3KSE; -.
PDBsum; 3OF8; -.
PDBsum; 3OF9; -.
PDBsum; 4AXL; -.
PDBsum; 4AXM; -.
PDBsum; 5F02; -.
PDBsum; 5I4H; -.
PDBsum; 5MAE; -.
PDBsum; 5MAJ; -.
PDBsum; 5MQY; -.
ProteinModelPortal; P07711; -.
SMR; P07711; -.
BioGrid; 107894; 23.
IntAct; P07711; 14.
MINT; MINT-3005764; -.
STRING; 9606.ENSP00000345344; -.
BindingDB; P07711; -.
ChEMBL; CHEMBL3837; -.
DrugBank; DB07477; BIPHENYL-4-YL-ACETALDEHYDE.
DrugBank; DB03661; Cysteinesulfonic Acid.
GuidetoPHARMACOLOGY; 2351; -.
MEROPS; I29.001; -.
iPTMnet; P07711; -.
PhosphoSitePlus; P07711; -.
BioMuta; CTSL; -.
DMDM; 115741; -.
EPD; P07711; -.
MaxQB; P07711; -.
PaxDb; P07711; -.
PeptideAtlas; P07711; -.
PRIDE; P07711; -.
TopDownProteomics; P07711; -.
DNASU; 1514; -.
Ensembl; ENST00000340342; ENSP00000365061; ENSG00000135047.
Ensembl; ENST00000343150; ENSP00000345344; ENSG00000135047.
GeneID; 1514; -.
KEGG; hsa:1514; -.
UCSC; uc004aph.4; human.
CTD; 1514; -.
DisGeNET; 1514; -.
EuPathDB; HostDB:ENSG00000135047.14; -.
GeneCards; CTSL; -.
H-InvDB; HIX0058839; -.
H-InvDB; HIX0170314; -.
HGNC; HGNC:2537; CTSL.
HPA; CAB000459; -.
MIM; 116880; gene.
neXtProt; NX_P07711; -.
OpenTargets; ENSG00000135047; -.
PharmGKB; PA162382890; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; P07711; -.
KO; K01365; -.
OMA; FRYIKDN; -.
OrthoDB; EOG091G0AKT; -.
PhylomeDB; P07711; -.
TreeFam; TF313739; -.
BRENDA; 3.4.22.15; 2681.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
EvolutionaryTrace; P07711; -.
GeneWiki; Cathepsin_L1; -.
GenomeRNAi; 1514; -.
PMAP-CutDB; P07711; -.
PRO; PR:P07711; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000135047; -.
CleanEx; HS_CTSL1; -.
ExpressionAtlas; P07711; baseline and differential.
Genevisible; P07711; HS.
GO; GO:0036021; C:endolysosome lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:BHF-UCL.
GO; GO:0005518; F:collagen binding; IDA:BHF-UCL.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
GO; GO:0001968; F:fibronectin binding; IPI:BHF-UCL.
GO; GO:0042393; F:histone binding; IDA:BHF-UCL.
GO; GO:0043394; F:proteoglycan binding; IPI:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0097655; F:serpin family protein binding; IPI:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEP:UniProtKB.
GO; GO:0019882; P:antigen processing and presentation; TAS:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; IDA:BHF-UCL.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0071888; P:macrophage apoptotic process; NAS:BHF-UCL.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
GO; GO:0045616; P:regulation of keratinocyte differentiation; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 17 {ECO:0000250|UniProtKB:P07154}.
PROPEP 18 113 Activation peptide.
/FTId=PRO_0000026244.
CHAIN 114 288 Cathepsin L1 heavy chain.
/FTId=PRO_0000026245.
PROPEP 289 291
/FTId=PRO_0000026246.
CHAIN 292 333 Cathepsin L1 light chain.
/FTId=PRO_0000026247.
ACT_SITE 138 138
ACT_SITE 276 276
ACT_SITE 300 300
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
DISULFID 135 178
DISULFID 169 211
DISULFID 269 322 Interchain (between heavy and light
chains).
CONFLICT 56 56 M -> V (in Ref. 6; AAH12612).
{ECO:0000305}.
CONFLICT 268 268 D -> N (in Ref. 7; AA sequence).
{ECO:0000305}.
HELIX 23 25 {ECO:0000244|PDB:1CS8}.
HELIX 26 35 {ECO:0000244|PDB:1CS8}.
HELIX 44 67 {ECO:0000244|PDB:1CS8}.
STRAND 72 75 {ECO:0000244|PDB:1CS8}.
TURN 79 82 {ECO:0000244|PDB:1CS8}.
HELIX 85 92 {ECO:0000244|PDB:1CS8}.
STRAND 103 105 {ECO:0000244|PDB:1CJL}.
HELIX 120 123 {ECO:0000244|PDB:2XU3}.
STRAND 134 136 {ECO:0000244|PDB:2XU3}.
HELIX 138 155 {ECO:0000244|PDB:2XU3}.
HELIX 163 169 {ECO:0000244|PDB:2XU3}.
TURN 171 174 {ECO:0000244|PDB:2XU3}.
HELIX 177 179 {ECO:0000244|PDB:2XU4}.
HELIX 183 193 {ECO:0000244|PDB:2XU3}.
STRAND 196 198 {ECO:0000244|PDB:2XU3}.
TURN 199 201 {ECO:0000244|PDB:2XU3}.
HELIX 215 217 {ECO:0000244|PDB:2XU3}.
STRAND 218 220 {ECO:0000244|PDB:2XU3}.
STRAND 223 227 {ECO:0000244|PDB:2XU3}.
HELIX 232 241 {ECO:0000244|PDB:2XU3}.
STRAND 245 249 {ECO:0000244|PDB:2XU3}.
HELIX 254 257 {ECO:0000244|PDB:2XU3}.
STRAND 261 264 {ECO:0000244|PDB:2XU3}.
STRAND 271 273 {ECO:0000244|PDB:4AXL}.
STRAND 276 285 {ECO:0000244|PDB:2XU3}.
STRAND 289 291 {ECO:0000244|PDB:2XU3}.
STRAND 294 299 {ECO:0000244|PDB:2XU3}.
STRAND 304 306 {ECO:0000244|PDB:3KSE}.
STRAND 311 315 {ECO:0000244|PDB:2XU3}.
STRAND 317 320 {ECO:0000244|PDB:2XU3}.
HELIX 321 323 {ECO:0000244|PDB:2XU3}.
TURN 324 326 {ECO:0000244|PDB:2XU3}.
STRAND 329 332 {ECO:0000244|PDB:2XU3}.
SEQUENCE 333 AA; 37564 MW; 8CD17D00EF859D85 CRC64;
MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA VWEKNMKMIE
LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP RKGKVFQEPL FYEAPRSVDW
REKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG
GLMDYAFQYV QDNGGLDSEE SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA
TVGPISVAID AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN
SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV


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